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B6IP82 (DAPF_RHOCS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diaminopimelate epimerase

Short name=DAP epimerase
EC=5.1.1.7
Gene names
Name:dapF
Ordered Locus Names:RC1_2197
OrganismRhodospirillum centenum (strain ATCC 51521 / SW) [Complete proteome] [HAMAP]
Taxonomic identifier414684 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan By similarity. HAMAP-Rule MF_00197

Catalytic activity

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate. HAMAP-Rule MF_00197

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1. HAMAP-Rule MF_00197

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00197.

Sequence similarities

Belongs to the diaminopimelate epimerase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondiaminopimelate epimerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291Diaminopimelate epimerase HAMAP-Rule MF_00197
PRO_1000124429

Regions

Region10 – 112Substrate binding By similarity
Region75 – 773Substrate binding By similarity
Region207 – 2082Substrate binding By similarity

Sites

Active site751Proton donor/acceptor By similarity
Active site2161Proton donor/acceptor By similarity
Binding site131Substrate By similarity
Binding site461Substrate By similarity
Binding site661Substrate By similarity
Binding site1561Substrate By similarity
Binding site1891Substrate By similarity
Site1581Important for catalytic activity By similarity
Site2071Important for catalytic activity By similarity

Amino acid modifications

Disulfide bond75 ↔ 216 HAMAP-Rule MF_00197

Sequences

Sequence LengthMass (Da)Tools
B6IP82 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 0B546D7062B5895C

FASTA29130,704
        10         20         30         40         50         60 
MVRRFLKMHG LGNDFVVLDA RRDPLPLTTA AARAIADRHT GVGCDQIVLL EPPRHPAADL 

        70         80         90        100        110        120 
FMRILNPDGS ESGACGNATR CVASLVADGS GRAEVTVETA TGLLRCRLRA DGSVTVDMGP 

       130        140        150        160        170        180 
ARLDWTQIPL AAAHDTLRVP AGAGPLQDAC CVGMGNPHAV FFVDDAEAVD LATLGPVLEH 

       190        200        210        220        230        240 
HSLFPQRCNI EVAQVLAPDH IRMRVWERGA GITRACGSGS CATLVAAARR GLTGRAAWIE 

       250        260        270        280        290 
LDGGRLWIEW HGDGHVLMTG PVATAFTGEL SETLLPGSLP SETPLPETVP A 

« Hide

References

[1]"Genome sequence of Rhodospirillum centenum."
Touchman J.W., Bauer C., Blankenship R.E.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51521 / SW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000613 Genomic DNA. Translation: ACI99584.1.
RefSeqYP_002298397.1. NC_011420.2.

3D structure databases

ProteinModelPortalB6IP82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING414684.RC1_2197.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI99584; ACI99584; RC1_2197.
GeneID7006965.
KEGGrce:RC1_2197.
PATRIC23319582. VBIRhoCen1465_2127.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0253.
HOGENOMHOG000220466.
KOK01778.
OMAKMRIFNN.
OrthoDBEOG6ND0M5.

Enzyme and pathway databases

BioCycRCEN414684:GHCM-2175-MONOMER.
UniPathwayUPA00034; UER00025.

Family and domain databases

HAMAPMF_00197. DAP_epimerase.
InterProIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERPTHR31689. PTHR31689. 1 hit.
PfamPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00652. DapF. 1 hit.
PROSITEPS01326. DAP_EPIMERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPF_RHOCS
AccessionPrimary (citable) accession number: B6IP82
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 16, 2008
Last modified: June 11, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways